1a4f | pdb_00001a4f
BAR-HEADED GOOSE HEMOGLOBIN (OXY FORM)
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Overview
We have determined the crystal structure of bar-headed goose haemoglobin, in the oxy form to a resolution of 2.0 A. The R-factor of the model is, 19.8%. The structure is similar to human HbA, but contacts between the, subunits show slightly altered packing of the tetramer. Bar-headed goose, blood shows a greatly elevated oxygen affinity compared to closely related, species of geese. This is apparently due to a single proline to alanine, mutation at the alpha 1 beta 1 interface which destabilises the T state of, the protein. The beta chain N and C termini are well-localized, and, together with other neighbouring basic groups they form a strongly, positively charged groove at the entrance to the central cavity around the, molecular dyad. The well-ordered conformation and the three-dimensional, distribution of positive charges clearly indicate this area to be the, inositol pentaphosphate binding site of bird haemoglobins.
About this Structure
1A4F is a Protein complex structure of sequences from Anser indicus with HEM and OXY as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form)., Zhang J, Hua Z, Tame JR, Lu G, Zhang R, Gu X, J Mol Biol. 1996 Jan 26;255(3):484-93. PMID:8568892
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